Hydrophobie forces are responsible for the folding of a highly potent natriuretic peptide analogue at a membrane mimetic surface: An NMR study

Biopolymers - Nucleic Acid Sciences Section

Volumn 42, Issue 1, 1997, Pages 37-48

  Carpenter, Katharine A ^a   Wilkes, Brian C ^a   De Lean, André ^a   Fournier, Alain ^a   Schiller, Peter W ^a  

^a CLIN RESEARCH INSTITUTE OF MONTREAL   (Canada)

Author keywords

Confonnational model of lipid boitnd atrial natriuretic peptide analogue; Molecular dynamics calculations; Nuclear overhauser effect distance constraints; Torsional angles

Indexed keywords

BIOLOGICAL MEMBRANES; COMPOSITION EFFECTS; COMPUTER SIMULATION; CONFORMATIONS; INTERFACES (MATERIALS); LIPIDS; MICELLES; MOLECULAR DYNAMICS; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLUTIONS;

DODECYLPHOSPHOCHOLINE MICELLES; HYDROPHOBIC INTERACTIONS; NATRIURETIC PEPTIDE ANALOGUE; NUCLEAR OVERHAUSER EFFECT; TORSIONAL ANGLE;

POLYPEPTIDES;

ARTICLE; HYDROPHOBICITY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PROTEIN FOLDING;

AMINO ACID SEQUENCE; ANIMALS; ATRIAL NATRIURETIC FACTOR; BRAIN; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NATRIURETIC PEPTIDE, BRAIN; NERVE TISSUE PROTEINS; PEPTIDE FRAGMENTS; PEPTIDES; PHOSPHOLIPIDS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RATS; SWINE;

EID: 0031195159     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-0282(199707)42:1<37::aid-bip4>3.0.co;2-2     Document Type: Article

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